Oxidation of a cysteine residue in elongation factor EF-Tu reversibly inhibits translation in the cyanobacterium Synechocystis sp. PCC 6803

Journal of Biological Chemistry

Volumn 291, Issue 11, 2016, Pages 5860-5870

  Yutthanasirikul, Rayakorn ^a   Nagano, Takanori ^a   Jimbo, Haruhiko ^a   Hihara, Yukako ^a   Kanamori, Takashi ^b,c   Ueda, Takuya ^c   Haruyama, Takamitsu ^d   Konno, Hiroki ^d   Yoshida, Keisuke ^e   Hisabori, Toru ^e   Nishiyama, Yoshitaka ^a  

^a SAITAMA UNIVERSITY   (Japan)

^b GeneFrontier Corporation   (Japan)

^c UNIVERSITY OF TOKYO   (Japan)

^d KANAZAWA UNIVERSITY   (Japan)

^e TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ATOMIC FORCE MICROSCOPY; COVALENT BONDS; ELONGATION; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; NUCLEOTIDES; SULFUR COMPOUNDS;

CYANOBACTERIUM SYNECHOCYSTIS; GEL-FILTRATION CHROMATOGRAPHY; INTERMOLECULAR DISULFIDE BOND; REACTIVE OXYGEN SPECIES; REDOX-DEPENDENT MANNER; SINGLE CYSTEINE RESIDUE; TRANSLATION SYSTEMS; TRANSLATIONAL ELONGATION;

OXIDATION;

CYSTEINE; DITHIOTHREITOL; ELONGATION FACTOR TU; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; HYDROGEN PEROXIDE; REACTIVE OXYGEN METABOLITE; SERINE; SULFENIC ACID; SULFUR DERIVATIVE; THIOREDOXIN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; DISULFIDE; NUCLEOTIDE; SULFENIC ACID DERIVATIVE;

ARTICLE; ATOMIC FORCE MICROSCOPY; BACTERIAL CELL; CHEMICAL STRUCTURE; COMPLEX FORMATION; CONTROLLED STUDY; DISULFIDE BOND; ESCHERICHIA COLI; GEL FILTRATION CHROMATOGRAPHY; IN VITRO STUDY; IN VIVO STUDY; MOLECULAR WEIGHT; MUTANT; NONHUMAN; OXIDATION; OXIDATION REDUCTION STATE; OXIDATIVE STRESS; PRIORITY JOURNAL; QUANTITATIVE ANALYSIS; SYNECHOCYSTIS; WILD TYPE; CHEMISTRY; METABOLISM; OXIDATION REDUCTION REACTION; PROTEIN SYNTHESIS;

BACTERIAL PROTEINS; CYSTEINE; DISULFIDES; HYDROGEN PEROXIDE; NUCLEOTIDES; OXIDATION-REDUCTION; PEPTIDE ELONGATION FACTOR TU; PROTEIN BIOSYNTHESIS; SULFENIC ACIDS; SYNECHOCYSTIS; THIOREDOXINS;

EID: 84964321585     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.706424     Document Type: Article

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